This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ji, H.
Right arrow Articles by Friedman, K. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ji, H.
Right arrow Articles by Friedman, K. L.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2005, p. 9103-9114, Vol. 25, No. 20
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.20.9103-9114.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Regulation of Telomere Length by an N-Terminal Region of the Yeast Telomerase Reverse Transcriptase{dagger}

Hong Ji, Margaret H. Platts, Latif M. Dharamsi,{ddagger} and Katherine L. Friedman*

Vanderbilt University, Department of Biological Sciences, VU Station B, Box 351634, Nashville, Tennessee 37235

Received 12 January 2005/ Returned for modification 7 March 2005/ Accepted 21 July 2005

Telomerase is a reverse transcriptase that maintains chromosome integrity through synthesis of repetitive telomeric sequences on the ends of eukaryotic chromosomes. In the yeast Saccharomyces cerevisiae, telomere length homeostasis is achieved through negative regulation of telomerase access to the chromosome terminus by telomere-bound Rap1 protein and its binding partners, Rif1p and Rif2p, and positive regulation by factors such as Ku70/80, Tel1p, and Cdc13p. Here we report the identification of mutations within an N-terminal region (region I) of the yeast telomerase catalytic subunit (Est2p) that cause telomere lengthening without altering measurable catalytic properties of the enzyme in vitro. These telomerase mutations affect telomere length through a Ku-independent mechanism and do not alter chromosome end structure. While Tel1p is required for expression of the telomere-lengthening phenotype, Rif1p and Rif2p are not, suggesting that telomere overextension is independent of Rap1p. Taken together, these data suggest that specific amino acids within region I of the catalytic subunit of yeast telomerase play a previously unanticipated role in the response to Tel1p regulation at the telomere.

* Corresponding author. Mailing address: Vanderbilt University, VU Station B, Box 351634, Nashville, TN 37235. Phone: (615) 322-5143. Fax: (615) 343-6707. E-mail: katherine.friedman{at}vanderbilt.edu.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} Present address: Emory University, Yerkes National Primate Research Center, 954 Gatewood Road NE, Atlanta, GA 30322.

Molecular and Cellular Biology, October 2005, p. 9103-9114, Vol. 25, No. 20
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.20.9103-9114.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zappulla, D. C., Roberts, J. N., Goodrich, K. J., Cech, T. R., Wuttke, D. S. (2009). Inhibition of yeast telomerase action by the telomeric ssDNA-binding protein, Cdc13p. Nucleic Acids Res 37: 354-367 [Abstract] [Full Text]  
  • Ji, H., Adkins, C. J., Cartwright, B. R., Friedman, K. L. (2008). Yeast Est2p Affects Telomere Length by Influencing Association of Rap1p with Telomeric Chromatin. Mol. Cell. Biol. 28: 2380-2390 [Abstract] [Full Text]  
  • Lue, N. F., Li, Z. (2007). Modeling and structure function analysis of the putative anchor site of yeast telomerase. Nucleic Acids Res 0: gkm531v1-10 [Abstract] [Full Text]  
  • Wyatt, H. D. M., Lobb, D. A., Beattie, T. L. (2007). Characterization of Physical and Functional Anchor Site Interactions in Human Telomerase. Mol. Cell. Biol. 27: 3226-3240 [Abstract] [Full Text]  
  • Xin, Z.-T., Beauchamp, A. D., Calado, R. T., Bradford, J. W., Regal, J. A., Shenoy, A., Liang, Y., Lansdorp, P. M., Young, N. S., Ly, H. (2007). Functional characterization of natural telomerase mutations found in patients with hematologic disorders. Blood 109: 524-532 [Abstract] [Full Text]  
  • Middleman, E. J., Choi, J., Venteicher, A. S., Cheung, P., Artandi, S. E. (2006). Regulation of Cellular Immortalization and Steady-State Levels of the Telomerase Reverse Transcriptase through Its Carboxy-Terminal Domain.. Mol. Cell. Biol. 26: 2146-2159 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»